Binding of more than one retinoid to visual opsins

Visual opsins bind 11-cis retinal at an orthosteric site to form rhodopsins but increasing evidence suggests that at least some are capable of binding an additional retinoid(s) at a separate, allosteric site(s). Microspectrophotometric measurements on isolated, dark-adapted, salamander photoreceptors indicated that the truncated retinal analog, β-ionone, partitioned into the membranes of green-sensitive rods; however, in blue-sensitive rod outer segments, there was an enhanced uptake of four or more β-ionones per rhodopsin. X-ray crystallography revealed binding of one β-ionone to bovine green-sensitive rod rhodopsin. Cocrystallization only succeeded with extremely high concentrations of β-ionone and binding did not alter the structure of rhodopsin from the inactive state. Salamander green-sensitive rod rhodopsin is also expected to bind β-ionone at sufficiently high concentrations because the binding site is present on its surface. Therefore, both blue- and green-sensitive rod rhodopsins have at least one allosteric binding site for retinoid, but β-ionone binds to the latter type of rhodopsin with low affinity and low efficacy.     

More than a monolayer: relating lung surfactant structure and mechanics to composition

Survanta, a clinically used bovine lung surfactant extract, in contact with surfactant in the subphase, shows a coexistence of discrete monolayer islands of solid phase coexisting with continuous multilayer "reservoirs" of fluid phase adjacent to the air-water interface. Exchange between the monolayer, the multilayer reservoir, and the subphase determines surfactant mechanical properties such as the monolayer collapse pressure and surface viscosity by regulating solid-fluid coexistence. Grazing incidence x-ray diffraction shows that the solid phase domains consist of two-dimensional crystals similar to those formed by mixtures of dipalmitoylphosphatidylcholine and palmitic acid. The condensed domains grow as the surface pressure is increased until they coalesce, trapping protrusions of liquid matrix. At approximately 40 mN/m, a plateau exists in the isotherm at which the solid phase fraction increases from approximately 60 to 90%, at which the surface viscosity diverges. The viscosity is driven by the percolation of the solid phase domains, which depends on the solid phase area fraction of the monolayer. The high viscosity may lead to high monolayer collapse pressures, help prevent atelectasis, and minimize the flow of lung surfactant out of the alveoli due to surface tension gradients.     

The latent trichophytosis of human clothing,II. Some data relating to Trichophyton pratense

Summary The author refers to the results of his investigations carried out with theT. pratense in 1940. He could continue these experiments only in the year 1965. This time he came to the conclusion that three fungi species:T. terrestre Durie &Frey,T. pratense andT. gypseum var.asteroides belong together. He could observe that the cultures of these fungi develop well on some kinds of textile materials. Relying upon these findings he applied the TO-KA-VA method in an inverted way to demonstrate the fungi which had settled on the textiles with the dust of soil. By means of this method he observed thatT. pratense had indeed occurred on some cloths. By further investigation he proved the identity ofT. terrestre Durie &Frey withT. pratense andT. gypseum var.asteroides and demonstrated, that this latter fungus might be the degenerative derivate of the former ones. Finally, he gave as his opinion that the settlement of theT. gypseum var.asteroides is also likely to occur on human clothing; however, far more rarely than that of other kinds of fungi.     

There's more than one way to scale a synapse

TNFalpha has been proposed to underlie synaptic scaling, but the mechanism and functional significance of this remain unclear. In this issue of Neuron, Cingolani et al. demonstrate that TNFalpha can mediate scaling through the regulation of beta3 integrins. Kaneko et al. show that TNFalpha-dependent synaptic scaling plays an important role in visual cortical plasticity.